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Protein

Protein kinase C-like 3

Gene

pkc-3

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Required for the normal progression of embryogenesis and viability of the organism. Plays an indispensable role in establishing embryonic polarity and in recruiting and maintaining par-6 to the periphery, through interaction with par-3. Required for epithelial cell polarity in the distal spermatheca. Phosphorylates serine residues of num-1.4 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.1 Publication

Cofactori

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei282 – 2821ATPPROSITE-ProRule annotationBy similarity
Active sitei377 – 3771Proton acceptorPROSITE-ProRule annotationBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri127 – 17751Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
BLAST
Nucleotide bindingi259 – 2679ATPPROSITE-ProRule annotationBy similarity

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • metal ion binding Source: UniProtKB-KW
  • protein domain specific binding Source: UniProtKB
  • protein kinase activity Source: WormBase
  • protein kinase C activity Source: UniProtKB-EC
  • protein serine/threonine kinase activity Source: UniProtKB

GO - Biological processi

  • asymmetric protein localization Source: WormBase
  • cell differentiation Source: UniProtKB-KW
  • defense response to fungus Source: WormBase
  • embryo development ending in birth or egg hatching Source: WormBase
  • establishment or maintenance of cell polarity Source: UniProtKB
  • gastrulation Source: UniProtKB-KW
  • gonadal mesoderm development Source: UniProtKB-KW
  • gonad development Source: UniProtKB
  • intracellular signal transduction Source: GO_Central
  • peptidyl-serine phosphorylation Source: WormBase
  • response to wounding Source: WormBase
  • single fertilization Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Differentiation, Fertilization, Gastrulation, Gonadal differentiation

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

ReactomeiR-CEL-5218921. VEGFR2 mediated cell proliferation.
SignaLinkiQ19266.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein kinase C-like 3 (EC:2.7.11.13)
Alternative name(s):
Atypical protein kinase C-3
Short name:
aPKC3
Gene namesi
Name:pkc-3Imported
Synonyms:aPKC
ORF Names:F09E5.1
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
Proteomesi
  • UP000001940 Componenti: Chromosome II

Organism-specific databases

WormBaseiF09E5.1; CE02604; WBGene00004034; pkc-3.

Subcellular locationi

  • Cytoplasm 2 Publications
  • Cytoplasmcytoskeleton 1 Publication

  • Note: Targeted and anchored at the apical surface (villi) of intestinal and pharyngeal cells, and in proximity with the cortical actin cytoskeleton that lies under the plasma membrane. Tightly bound to organelles/cytoskeleton in six of the seven developmental stages. Accumulation in cytoplasm is restricted to L1 larvae and adults. Colocalized with par-3 at the anterior cortex of the 1-cell embryo.2 Publications

GO - Cellular componenti

  • apical plasma membrane Source: WormBase
  • cell cortex Source: WormBase
  • cortical actin cytoskeleton Source: UniProtKB
  • cytosol Source: WormBase
  • membrane Source: WormBase
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Disruption phenotypei

Worms show defects in embryogenesis. Mutant embryos show defects in their polarity and cleavage patterns which disrupt hatching.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi214 – 2141I → A: Prevents binding with num-1 (isoform a and isoform c). 1 Publication
Mutagenesisi216 – 2161N → A: Prevents binding with num-1 (isoform a and isoform c). 1 Publication
Mutagenesisi219 – 2191F → A: Prevents binding with num-1 (isoform a and isoform c). 1 Publication
Mutagenesisi222 – 2221H → A: No effect on binding with num-1 (isoform a and isoform c). 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 597597Protein kinase C-like 3PRO_0000055737Add
BLAST

Proteomic databases

EPDiQ19266.
PaxDbiQ19266.

PTM databases

iPTMnetiQ19266.

Expressioni

Tissue specificityi

Abundantly expressed in the anterior and posterior pharyngeal bulbs, the pharyngeal-intestinal valve, vulval cells, and a region at the posterior end of the intestine that corresponds to site of co-assembly of the intestinal-rectal valve and anal sphincter, and depressor muscles. Modest expression apparent in four hypodermal cells that provide cuticle and muscle anchorage in the tail. Strong expression observed in discrete patches and spots in vulval cells and in somatic cells of the spermatheca. Transiently coexpressed and colocalized with par-6 and par-3, asymmetrically in the developing somatic gonad, including the spermathecal precursor cells of L4 larvae.3 Publications

Developmental stagei

Expressed throughout development, at highest level in the L1 stage and lowest in L3. Peripheral staining pattern in early embryos. The staining in 1-cell embryos is weak and uniform just after the completion of meiosis, but increases in intensity and becomes concentrated at the anterior periphery during pronuclear migration. The peripheral staining becomes restricted to about 50% embryo length during the pronuclear meeting and pronuclear fusion stage. By early anaphase, the staining extends posteriorly beyond the midline of the zygote and covers about 60% of the total length of embryos. In 2- and 4-cell stages, staining is uniform at the periphery of the AB cell, its daughters and the EMS cell, but peripheral staining in P1 and P2 is restricted to the boundaries with other blastomeres.2 Publications

Interactioni

Subunit structurei

Interaction with par-3 required for the peripheral localization of par-6 and to form a par-3/par-6/pkc-3 complex, which is activated when cdc-42 interacts with par-6. Binds avidly to the phosphotyrosine interaction domain (PID) of a novel pkc-3 adapter protein num-1, which enables tethering and targeting of pkc-3 to the cell periphery.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
num-1Q9XTY65EBI-319158,EBI-495781
num-1Q9XTY6-15EBI-319158,EBI-495798
par-3Q173533EBI-319158,EBI-321762
par-6Q9NAN24EBI-319158,EBI-318782

GO - Molecular functioni

  • protein domain specific binding Source: UniProtKB

Protein-protein interaction databases

BioGridi39258. 3 interactions.
DIPiDIP-24814N.
IntActiQ19266. 3 interactions.
MINTiMINT-1112545.
STRINGi6239.F09E5.1.2.

Structurei

3D structure databases

ProteinModelPortaliQ19266.
SMRiQ19266. Positions 13-93, 126-589.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini12 – 9584PB1PROSITE-ProRule annotationAdd
BLAST
Domaini253 – 522270Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini524 – 59572AGC-kinase C-terminalAdd
BLAST

Domaini

Residues 212-224 are capable of binding the PID domain of num-1 isoform a and isoform c.

Sequence similaritiesi

Contains 1 AGC-kinase C-terminal domain.Curated
Contains 1 PB1 domain.PROSITE-ProRule annotation
Contains 1 phorbol-ester/DAG-type zinc finger.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri127 – 17751Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG0695. Eukaryota.
ENOG410ZMG2. LUCA.
GeneTreeiENSGT00820000126964.
HOGENOMiHOG000233033.
InParanoidiQ19266.
KOiK06069.
OMAiSSKWAVS.
OrthoDBiEOG7HF1J3.
PhylomeDBiQ19266.

Family and domain databases

InterProiIPR000961. AGC-kinase_C.
IPR020454. DAG/PE-bd.
IPR011009. Kinase-like_dom.
IPR000270. PB1_dom.
IPR002219. PE/DAG-bd.
IPR012233. PKC.
IPR017892. Pkinase_C.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00130. C1_1. 1 hit.
PF00564. PB1. 1 hit.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]
PIRSFiPIRSF000554. PKC_zeta. 1 hit.
PRINTSiPR00008. DAGPEDOMAIN.
SMARTiSM00109. C1. 1 hit.
SM00666. PB1. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS51285. AGC_KINASE_CTER. 1 hit.
PS51745. PB1. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS00479. ZF_DAG_PE_1. 1 hit.
PS50081. ZF_DAG_PE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q19266-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSPTSLEED GDIKLKTRFQ GQVVVLYARP PLILDDFFAL LKDACKQHKK
60 70 80 90 100
QDITVKWIDE DGDPISIDSQ MELDEAVRCL NSSQEAELNI HVFVGKPELP
110 120 130 140 150
GLPCQGEDKT VYRRGARRWK KIYLYNGHRF QAKRLNRRIQ CFICHDYIWG
160 170 180 190 200
IGRQGFRCVD CRLCVHKKCH RHVRTHCGQA LQGPNIIPMA PASGSLKGAR
210 220 230 240 250
SNTSSSTTRS GGGIDNGAFH EHEIESPGST SHDASRAMNG NGSSKWAVSL
260 270 280 290 300
NDFRLLTVIG RGSYAKVVQA EHVSTRQIYA IKIIKKEMFN EDEDIDWVQT
310 320 330 340 350
EKSVFEAASN YPFLVGLHSC FQTESRLFFV IEFVPGGDLM FHMQQQRKLP
360 370 380 390 400
EEHARFYSGE IILALHFLHS RGIIYRDLKL DNVLIDAEGH IKLTDYGMCK
410 420 430 440 450
ENIKDGDLTS TFCGTPNYIA PEILRGDEYG FSVDWWALGV LMFEMMAGRS
460 470 480 490 500
PFDIVGMQNS EENTEDYLFQ IILERQIRIP RSLSVRASGI LKGFLNKDPT
510 520 530 540 550
ERLGCKLDIN EGLRDMKEHQ FFRGFIDWEA LEQKAVAPPY HPAVESDRDL
560 570 580 590
THFDHQFTDE LPQLSPDNPD VIARIDQSEF DGFEYVNPLQ MSREDSV
Length:597
Mass (Da):68,035
Last modified:November 1, 1996 - v1
Checksum:iA92760E880DB11B8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB007320 mRNA. Translation: BAF80143.1.
AF025666 mRNA. Translation: AAB88885.1.
FO081044 Genomic DNA. Translation: CCD68754.1.
PIRiT16006.
RefSeqiNP_495011.1. NM_062610.6.
UniGeneiCel.19483.

Genome annotation databases

EnsemblMetazoaiF09E5.1; F09E5.1; WBGene00004034.
GeneIDi173914.
KEGGicel:CELE_F09E5.1.
UCSCiF09E5.1.2. c. elegans.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB007320 mRNA. Translation: BAF80143.1.
AF025666 mRNA. Translation: AAB88885.1.
FO081044 Genomic DNA. Translation: CCD68754.1.
PIRiT16006.
RefSeqiNP_495011.1. NM_062610.6.
UniGeneiCel.19483.

3D structure databases

ProteinModelPortaliQ19266.
SMRiQ19266. Positions 13-93, 126-589.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi39258. 3 interactions.
DIPiDIP-24814N.
IntActiQ19266. 3 interactions.
MINTiMINT-1112545.
STRINGi6239.F09E5.1.2.

PTM databases

iPTMnetiQ19266.

Proteomic databases

EPDiQ19266.
PaxDbiQ19266.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiF09E5.1; F09E5.1; WBGene00004034.
GeneIDi173914.
KEGGicel:CELE_F09E5.1.
UCSCiF09E5.1.2. c. elegans.

Organism-specific databases

CTDi173914.
WormBaseiF09E5.1; CE02604; WBGene00004034; pkc-3.

Phylogenomic databases

eggNOGiKOG0695. Eukaryota.
ENOG410ZMG2. LUCA.
GeneTreeiENSGT00820000126964.
HOGENOMiHOG000233033.
InParanoidiQ19266.
KOiK06069.
OMAiSSKWAVS.
OrthoDBiEOG7HF1J3.
PhylomeDBiQ19266.

Enzyme and pathway databases

ReactomeiR-CEL-5218921. VEGFR2 mediated cell proliferation.
SignaLinkiQ19266.

Miscellaneous databases

PROiQ19266.

Family and domain databases

InterProiIPR000961. AGC-kinase_C.
IPR020454. DAG/PE-bd.
IPR011009. Kinase-like_dom.
IPR000270. PB1_dom.
IPR002219. PE/DAG-bd.
IPR012233. PKC.
IPR017892. Pkinase_C.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00130. C1_1. 1 hit.
PF00564. PB1. 1 hit.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]
PIRSFiPIRSF000554. PKC_zeta. 1 hit.
PRINTSiPR00008. DAGPEDOMAIN.
SMARTiSM00109. C1. 1 hit.
SM00666. PB1. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS51285. AGC_KINASE_CTER. 1 hit.
PS51745. PB1. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS00479. ZF_DAG_PE_1. 1 hit.
PS50081. ZF_DAG_PE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Atypical protein kinase C cooperates with PAR-3 to establish embryonic polarity in Caenorhabditis elegans."
    Tabuse Y., Izumi Y., Piano F., Kemphues K.J., Miwa J., Ohno S.
    Development 125:3607-3614(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH PAR-3, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
    Strain: Bristol N2.
    Tissue: Embryo1 Publication.
  2. "Structure, expression, and properties of an atypical protein kinase C (PKC3) from Caenorhabditis elegans. PKC3 is required for the normal progression of embryogenesis and viability of the organism."
    Wu S.-L., Staudinger J., Olson E.N., Rubin C.S.
    J. Biol. Chem. 273:1130-1143(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    Strain: Bristol N2Imported.
  3. "Genome sequence of the nematode C. elegans: a platform for investigating biology."
    The C. elegans sequencing consortium
    Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Bristol N2.
  4. "PAR-6 is a conserved PDZ domain-containing protein that colocalizes with PAR-3 in Caenorhabditis elegans embryos."
    Hung T.-J., Kemphues K.J.
    Development 126:127-135(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PAR-3 AND PAR-6, TISSUE SPECIFICITY.
    Strain: Bristol N21 Publication.
    Tissue: Embryo1 Publication.
  5. "CDC-42 controls early cell polarity and spindle orientation in C. elegans."
    Gotta M., Abraham M.C., Ahringer J.
    Curr. Biol. 11:482-488(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CDC-42.
    Strain: Bristol N21 Publication.
    Tissue: Embryo1 Publication.
  6. "A novel adapter protein employs a phosphotyrosine binding domain and exceptionally basic N-terminal domains to capture and localize an atypical protein kinase C: characterization of Caenorhabditis elegans C kinase adapter 1, a protein that avidly binds protein kinase C3."
    Zhang L., Wu S.-L., Rubin C.S.
    J. Biol. Chem. 276:10463-10475(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NUM-1.
    Strain: Bristol N21 Publication.
  7. "Structural properties and mechanisms that govern association of C kinase adapter 1 with protein kinase C3 and the cell periphery."
    Zhang L., Wu S.-L., Rubin C.S.
    J. Biol. Chem. 276:10476-10484(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NUM-1, MUTAGENESIS OF ILE-214; ASN-216; PHE-219 AND HIS-222.
  8. "PAR-3 is required for epithelial cell polarity in the distal spermatheca of C. elegans."
    Aono S., Legouis R., Hoose W.A., Kemphues K.J.
    Development 131:2865-2874(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.

Entry informationi

Entry nameiKPC3_CAEEL
AccessioniPrimary (citable) accession number: Q19266
Secondary accession number(s): A7VJC8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: November 1, 1996
Last modified: July 6, 2016
This is version 147 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.